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Mechanotransduction Mechanisms of Hypertrophy and Performance with Resistance Exercise
Published in Peter M. Tiidus, Rebecca E. K. MacPherson, Paul J. LeBlanc, Andrea R. Josse, The Routledge Handbook on Biochemistry of Exercise, 2020
Andrew C. Fry, Justin X. Nicoll, Luke A. Olsen
Eccentric exercise produces a rapid decrease in the cytoskeletal protein desmin immediately following resistance exercise, with a subsequent 3-fold increase 5–7 days later (5). Woolstenhulme et al. (182) similarly showed a gradual increase in desmin content each week of an 8-week training intervention. The muscle fibre transmembrane protein α7β1 integrin also increases following traditional resistance exercise (13). This increase in structural proteins is necessary to equip the muscle fibre with heightened structural integrity for further force propagation, as demonstrated with conditional knockout models revealing augmented force transmission and biochemical signalling characteristics. Indeed, the ECM similarly undergoes rapid remodelling following a mechanical stimulus in a temporal manner. Initially, matrix metalloproteinases (MMPs), protein-degrading enzymes within the ECM, increase in abundance largely to allow necessary migration of the fibroblast, satellite cell, and macrophages. Following this acute rise in MMP concentration, tissue inhibitors of metalloproteinases (TIMPs) are elevated to inhibit MMPs (89, 107). A concomitant increase in ECM proteins, such as multiple isoforms of collagen, are synthesized within both the muscle fibre and surrounding cells and are exported to the ECM to provide further structural integrity. This enhanced protein content of the ECM, muscle fibre membrane, cytoskeleton, and nuclear membrane allow for an improved means of rapid communication via biophysical force propagation.
The Role of Oncostatin M in The Acute Phase Response
Published in Andrzej Mackiewicz, Irving Kushner, Heinz Baumann, Acute Phase Proteins, 2020
Carl D. Richards, Mohammed Shoyab
A striking feature of the acute phase proteins induced by OM, IL-6, and LIF in hepatocytes is that many are antiproteinase in action.22-24 A major antiprotease of connective tissue cells is termed TIMP (tissue inhibitor of metalloproteinases) because of the potent inhibitory activity of its metalloproteinase enzyme function. TIMP thus plays a role in the extracellular matrix (ECM) metabolism of normal physiological processes as well as in the pathological breakdown of ECM in chronic inflammation and tumor metastasis.25-27 We have examined TIMP-1 expression in Hep G2 cells as well as fibroblast cultures and found that OM potently enhances TIMP-1 mRNA levels and protein production (Figure 3).36 Both cell types show marked enhancement due to OM stimulation, even though basal levels of TIMP- 1 mRNA are much greater in fibroblasts (Figure 3). Also, OM was far more potent in enhancing TIMP-1 than IL-6 or LIF.36 This suggests that OM is a potent regulator of antiproteinase expression not only in hepatocytes, but also in connective tissue cells from extrahepatic sites. The induction of tissue site antiproteases by OM, IL-6, and LIF may well prove to be important in the modulation of local responses at sites of inflammation.
Metastasis
Published in Victor A. Bernstam, Pocket Guide to GENE LEVEL DIAGNOSTICS in Clinical Practice, 2019
The opposite effect on the invasive phenotype can be seen in the expression of proteinase inhibitors. A group of tissue inhibitors of metalloproteinases (TIMPs) may function as metastasis suppressors and the degree of their expression can also characterize the metastatic potential of a given tumor.
Association of VEGFA, TIMP-3, and IL-6 gene polymorphisms with predisposition to optic neuritis and optic neuritis with multiple sclerosis
Published in Ophthalmic Genetics, 2021
Vaida Punyte, Alvita Vilkeviciute, Greta Gedvilaite, Loresa Kriauciuniene, Rasa Liutkeviciene
TIMP-3 belongs to the family of tissue inhibitors of metalloproteinases (TIMP) (19). During inflammation, the balance between matrix metalloproteinases (MMPs) and TIMPs is crucial. Some MMPs contribute to the release of pro-inflammatory cytokines. Specific MMP ADAM-17 is responsible for the release of tumor necrosis factors (TNFs) from their transmembrane progenitors (20). Cytokines of the TNF family are pro-inflammatory and pro-apoptotic and ADAM-17 increases their systemic bioavailability. TIMP-3 inhibits the inflammatory response by limiting the release of TNFs (21). Other MMPs contribute to the development of neuroinflammatory diseases such as ON and MS (22). It has been shown that the secretion of MMP-9 is increased during inflammation and together with MMP-2 they contribute to the collapse of the BBB (23). SNPs in this gene are associated with the development of oral cancer (24) and breast cancer (25).
Lunasin abrogates the expression of matrix metalloproteinases and reduction of type II collagen
Published in Artificial Cells, Nanomedicine, and Biotechnology, 2019
Weihua Dai, Zhiyong Liang, Hongbo Liu, Guangzong Zhao, Chunfang Ju
Osteoarthritis (OA) is commonly seen in the elderly, and it affects millions of the population worldwide. Multiple biochemical and mechanical factors contribute to the initiation of OA [1]. Mild inflammation associated with overproduction of IL-1β plays a critical role in the pathological progression of OA. IL-1β results in the induction of matrix metalloproteinases (MMPs) and nitric oxide (NO) in chondrocytes. MMPs have been recognized as crucial factors in OA [2]. Among them, MMP-3 and MMP-13 act as the two most important collagenases involved in the degradation of the cartilage matrix in OA [3]. MMP-3 can cleave multiple extracellular matrices including proteoglycans [4]. MMP-13 is responsible for the digestion of type II collagen [5,6]. The physiological activities of MMPs are antagonized by tissue inhibitors of metalloproteinases (TIMPs), such as TIMP-1 and TIMP-2 [7]. Inhibiting the activity of MMPs and degradation of ECM has become a promising strategy to blunt OA progression.
Peptide PD29 treats bleomycin-induced pulmonary fibrosis by inhibiting the TGF-β/smad signaling pathway
Published in Experimental Lung Research, 2019
Qingbo Sun, Jialiang Hu, Pengcheng Yu, Zhaohao Zhu, Ruihe Yu, Chuang Ge, Chencheng Li, Guiyue Wu, Bingjing Lin, Guangpan Liu, Meng Liu, Huan Bian, Hanmei Xu, Shaochang Jia
The ECM plays a supporting role by bridging cells and tissues. Matrix metalloproteinases (MMP) can modulate the dynamic balance between degradation and recombination of ECM by separating its components to eliminate certain specific signals, reveal hidden signals, and even modify biological activities. Various substances are released or activated, intervening various morphological and functional changes in cells and tissues.18–19 MMP are important enzymes in the regulation of ECM metabolism, and their degradation can be inhibited by specific molecules termed tissue inhibitors of metalloproteinases (TIMP).20–21 Metabolic disorders of the ECM are involved in the pathophysiological processes of acute and chronic PF, which renders MMP and their inhibitors invaluable in the study of PF. MMP/TIMP banlance appears to be disrupted in PF, which causes repeated destruction, abnormal repair and excessive accumulation of ECM.22–23